Effect of plasmid replication deregulation via inc mutations on E. coli proteome & simple flux model analysis
Jonathan Meadea b, Patrick Bartlowc d, Ram Narayan Trivedie f, Parvez Akhtarf g, Mohammad M. Ataaid h, Saleem Ahmad Khanf i, Michael M. Domachb j✉
- aDepartment Chemical Engineering, Carnegie Mellon University, 15213, Pittsburgh, PA, USA. jwmeade@andrew.cmu.edu
- bDepartment Chemical Engineering, Carnegie Mellon University, 15213, Pittsburgh, PA, USA
- cDepartment Chemical Engineering, University of Pittsburgh, 15219, Pittsburgh, PA, USA. pab66@pitt.edu
- dDepartment Chemical Engineering, University of Pittsburgh, 15219, Pittsburgh, PA, USA
- eMicrobiology & Molecular Genetics, University of Pittsburgh School of Medicine, 15219, Pittsburgh, PA, USA. rnt88@pitt.edu
- fMicrobiology & Molecular Genetics, University of Pittsburgh School of Medicine, 15219, Pittsburgh, PA, USA
- gMicrobiology & Molecular Genetics, University of Pittsburgh School of Medicine, 15219, Pittsburgh, PA, USA. paa13@pitt.edu
- hDepartment Chemical Engineering, University of Pittsburgh, 15219, Pittsburgh, PA, USA. ataai@pitt.edu
- iMicrobiology & Molecular Genetics, University of Pittsburgh School of Medicine, 15219, Pittsburgh, PA, USA. Khan@pitt.edu
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Abstract
When the replication of a plasmid based on sucrose selection is deregulated via the inc1 and inc2 mutations, high copy numbers (7,000 or greater) are attained while the growth rate on minimal medium is negligibly affected. Adaptions were assumed to be required in order to sustain the growth rate. Proteomics indicated that indeed a number of adaptations occurred that included increased expression of ribosomal proteins and 2-oxoglutarate dehydrogenase. The operating space prescribed by a basic flux model that maintained phenotypic traits (e.g. growth, byproducts, etc.) within typical bounds of resolution was consistent with the flux implications of the proteomic changes.
TL;DRProteomics indicated that indeed a number of adaptations occurred that included increased expression of ribosomal proteins and 2-oxoglutarate dehydrogenase, consistent with the flux implications of the proteomic changes. (Semantic Scholar)